메뉴 건너뛰기




Volumn 319, Issue 3, 2004, Pages 787-794

Crystal structure of the ribonuclease P protein Ph1877p from hyperthermophilic archaeon Pyrococcus horikoshii OT3

Author keywords

Archaea; Crystal structure; Pre tRNA; Pyrococcus horikoshii; Ribonuclease P; RNA binding site; Site directed mutagenesis

Indexed keywords

BACTERIAL PROTEIN; CYTOSINE DEAMINASE; ISOPROTEIN; PROTEIN PH1877P; RIBONUCLEASE P; UNCLASSIFIED DRUG;

EID: 2942627587     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.05.055     Document Type: Article
Times cited : (45)

References (28)
  • 1
    • 0021013526 scopus 로고
    • The RNA moiety of ribonuclease P is the catalytic subunit of the enzyme
    • Guerrier-Takada C., Gardiner K., Marsh T., Pace N., Altman S. The RNA moiety of ribonuclease P is the catalytic subunit of the enzyme. Cell. 35:1983;849-857
    • (1983) Cell , vol.35 , pp. 849-857
    • Guerrier-Takada, C.1    Gardiner, K.2    Marsh, T.3    Pace, N.4    Altman, S.5
  • 2
    • 0036210354 scopus 로고    scopus 로고
    • Human ribonuclease P: Subunits, function, and intranuclear localization
    • Jarrous N. Human ribonuclease P: subunits, function, and intranuclear localization. RNA. 8:2002;1-7
    • (2002) RNA , vol.8 , pp. 1-7
    • Jarrous, N.1
  • 3
    • 0028962136 scopus 로고
    • Evolutionary perspective on the structure and function of ribonuclease P, a ribozyme
    • Pace N.R., Brown J.W. Evolutionary perspective on the structure and function of ribonuclease P, a ribozyme. J. Bacteriol. 177:1995;1919-1928
    • (1995) J. Bacteriol. , vol.177 , pp. 1919-1928
    • Pace, N.R.1    Brown, J.W.2
  • 4
    • 0031711821 scopus 로고    scopus 로고
    • Ribonuclease P: Unity and diversity in a tRNA processing ribozyme
    • Frank D.N., Pace N.R. Ribonuclease P: unity and diversity in a tRNA processing ribozyme. Annu. Rev. Biochem. 67:1998;153-180
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 153-180
    • Frank, D.N.1    Pace, N.R.2
  • 5
    • 0024654339 scopus 로고
    • Identification and characterization of an RNA molecule that copurifies with RNase P activity from HeLa cells
    • Bartkiewicz M., Gold H., Altman S. Identification and characterization of an RNA molecule that copurifies with RNase P activity from HeLa cells. Genes Dev. 3:1989;488-499
    • (1989) Genes Dev. , vol.3 , pp. 488-499
    • Bartkiewicz, M.1    Gold, H.2    Altman, S.3
  • 6
    • 0028817431 scopus 로고
    • Substrate recognition by human RNase P: Identification of small, model substrates for the enzyme
    • Yuan Y., Altman S. Substrate recognition by human RNase P: identification of small, model substrates for the enzyme. EMBO J. 14:1995;159-168
    • (1995) EMBO J. , vol.14 , pp. 159-168
    • Yuan, Y.1    Altman, S.2
  • 7
    • 0035127579 scopus 로고    scopus 로고
    • Eukaryotic ribonuclease P: Increased complexity to cope with the nuclear pre-tRNA pathway
    • Xiao S., Houser-Scott F., Engelke D.R. Eukaryotic ribonuclease P: increased complexity to cope with the nuclear pre-tRNA pathway. J. Cell Physiol. 187:2001;11-20
    • (2001) J. Cell Physiol. , vol.187 , pp. 11-20
    • Xiao, S.1    Houser-Scott, F.2    Engelke, D.R.3
  • 8
    • 0025357508 scopus 로고
    • Characterization of ribonuclease P from the archaebacterium Sulfolobus solfataricus
    • Darr S.C., Pace B., Pace N.R. Characterization of ribonuclease P from the archaebacterium Sulfolobus solfataricus. J. Biol. Chem. 265:1990;12927-12932
    • (1990) J. Biol. Chem. , vol.265 , pp. 12927-12932
    • Darr, S.C.1    Pace, B.2    Pace, N.R.3
  • 9
    • 0025992792 scopus 로고
    • The RNA component of RNase P from the archaebacterium Haloferax volcanii
    • Nieuwlandt D.T., Haas E.S., Daniels C.J. The RNA component of RNase P from the archaebacterium Haloferax volcanii. J. Biol. Chem. 266:1991;5689-5695
    • (1991) J. Biol. Chem. , vol.266 , pp. 5689-5695
    • Nieuwlandt, D.T.1    Haas, E.S.2    Daniels, C.J.3
  • 10
    • 0034826649 scopus 로고    scopus 로고
    • Characterization of RNase P holoenzymes from Methanococcus jannaschii and Methanothermobacter thermoautotrophicus
    • Andrews A.J., Hall T.A., Brown J.W. Characterization of RNase P holoenzymes from Methanococcus jannaschii and Methanothermobacter thermoautotrophicus. Biol. Chem. 382:2001;1171-1177
    • (2001) Biol. Chem. , vol.382 , pp. 1171-1177
    • Andrews, A.J.1    Hall, T.A.2    Brown, J.W.3
  • 14
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:1997;307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 17
    • 0029137828 scopus 로고
    • The structure and evolution of alpha/beta barrel proteins
    • Reardon D., Farber G.K. The structure and evolution of alpha/beta barrel proteins. FASEB J. 9:1995;497-502
    • (1995) FASEB J. , vol.9 , pp. 497-502
    • Reardon, D.1    Farber, G.K.2
  • 18
    • 0032076249 scopus 로고    scopus 로고
    • Ribonuclease P protein structure: Evolutionary origins in the translational apparatus
    • Stams T., Niranjanakumari S., Fierke C.A., Christianson D.W. Ribonuclease P protein structure: evolutionary origins in the translational apparatus. Science. 280:1998;752-755
    • (1998) Science , vol.280 , pp. 752-755
    • Stams, T.1    Niranjanakumari, S.2    Fierke, C.A.3    Christianson, D.W.4
  • 19
    • 0034614360 scopus 로고    scopus 로고
    • The structure of ribonuclease P protein from Staphylococcus aureus reveals a unique binding site for single-stranded RNA
    • Spitzfaden C., Nicholson N., Jones J.J., Guth S., Lehr R., Prescott C.D. The structure of ribonuclease P protein from Staphylococcus aureus reveals a unique binding site for single-stranded RNA. J. Mol. Biol. 295:2000;105-115
    • (2000) J. Mol. Biol. , vol.295 , pp. 105-115
    • Spitzfaden, C.1    Nicholson, N.2    Jones, J.J.3    Guth, S.4    Lehr, R.5    Prescott, C.D.6
  • 22
    • 0020653505 scopus 로고
    • Structure, biosynthesis, and function of queuosine in transfer RNA
    • Nishimura S. Structure, biosynthesis, and function of queuosine in transfer RNA. Prog. Nucleic Acid Res. Mol. Biol. 28:1983;49-73
    • (1983) Prog. Nucleic Acid Res. Mol. Biol. , vol.28 , pp. 49-73
    • Nishimura, S.1
  • 23
    • 0029991713 scopus 로고    scopus 로고
    • Crystal structure of tRNA-guanine transglycosylase: RNA modification by base exchange
    • Romier C., Reuter K., Suck D., Ficner R. Crystal structure of tRNA-guanine transglycosylase: RNA modification by base exchange. EMBO J. 15:1996;2850-2857
    • (1996) EMBO J. , vol.15 , pp. 2850-2857
    • Romier, C.1    Reuter, K.2    Suck, D.3    Ficner, R.4
  • 24
    • 0141596159 scopus 로고    scopus 로고
    • Chemical trapping and crystal structure of a catalytic tRNA guanine transglycosylase covalent intermediate
    • Xianjun W.X., Huang R.H. Chemical trapping and crystal structure of a catalytic tRNA guanine transglycosylase covalent intermediate. Nat. Struc. Biol. 10:2003;781-788
    • (2003) Nat. Struc. Biol. , vol.10 , pp. 781-788
    • Xianjun, W.X.1    Huang, R.H.2
  • 25
    • 0029935208 scopus 로고    scopus 로고
    • Comparative analysis of ribonuclease P RNA using gene sequences from natural microbial populations reveals tertiary structural elements
    • Brown J.W., Nolan J.M., Haas E.S., Rubio M.A., Major F., Pace N.R. Comparative analysis of ribonuclease P RNA using gene sequences from natural microbial populations reveals tertiary structural elements. Proc. Natl. Acad. Sci. USA. 93:1996;3001-3006
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 3001-3006
    • Brown, J.W.1    Nolan, J.M.2    Haas, E.S.3    Rubio, M.A.4    Major, F.5    Pace, N.R.6
  • 26
    • 0031588542 scopus 로고    scopus 로고
    • Remarkable morphological variability of a common RNA folding motif: The GNRA tetraloop-receptor interaction
    • Abramovitz D.L., Pyle A.M. Remarkable morphological variability of a common RNA folding motif: the GNRA tetraloop-receptor interaction. J. Mol. Biol. 266:1997;493-506
    • (1997) J. Mol. Biol. , vol.266 , pp. 493-506
    • Abramovitz, D.L.1    Pyle, A.M.2
  • 27
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W., Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers. 22:1983;2577-2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 28
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K., Honing B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins. 11:1991;281-296
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.2    Honing, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.